Research workbench
Structure of HAMP(AF1503)-tsr fusion - hamp (A291V) mutant
Analyse Structure of HAMP(AF1503)-tsr fusion - hamp (A291V) mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZX6
- Type
- protein
- Length
- 606 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hamp, methyl-accepting chemotaxis protein I
- UniProt
- O28769, P02942
- Ligands
- CL
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 90% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hamp, methyl-accepting chemotaxis protein I | protein | 303 | 89% helix, 1% strand | O28769, P02942 |
| B | Hamp, methyl-accepting chemotaxis protein I | protein | 303 | 91% helix, 0% strand | O28769, P02942 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 115 | 0.62 | 0.87 | 24 | empty |
| 2 | 209 | 0.57 | 0.80 | 38 | empty |
| 3 | 66 | 0.42 | 0.81 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 5887 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 3ZX6 · Structure of Hamp(AF1503)-Tsr fusion - Hamp (A291V) mutant · the same entry in another collection · chain B against B, TM-score 1.00
- P02942 · AlphaFold monomer V2.0 prediction for methyl-accepting chemotaxis protein I (P02942) · a predicted model of the same protein · chain A against A, TM-score 0.90
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O28769
- Every structure of UniProt P02942
- Elsewhere: RCSB PDB 3ZX6 · PDBe 3ZX6 · UniProt O28769 · UniProt P02942
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